Abstract
The complex between the DnaB helicase and the DnaG primase unwinds duplex DNA at the eubacterial replication fork and synthesizes the Okazaki RNA primers. The crystal structures of hexameric DnaB and its complex with the helicase binding domain (HBD) of DnaG reveal that within the hexamer the two domains of DnaB pack with strikingly different symmetries to form a distinct two-layered ring structure. Each of three bound HBDs stabilizes the DnaB hexamer in a conformation that may increase its processivity. Three positive, conserved electrostatic patches on the N-terminal domain of DnaB may also serve as a binding site for DNA and thereby guide the DNA to a DnaG active site.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 459-463 |
| Number of pages | 5 |
| Journal | Science |
| Volume | 318 |
| Issue number | 5849 |
| DOIs | |
| State | Published - Oct 19 2007 |
| Externally published | Yes |
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Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase. / Bailey, Scott; Eliason, William K.; Steitz, Thomas A.
In: Science, Vol. 318, No. 5849, 19.10.2007, p. 459-463.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase
AU - Bailey, Scott
AU - Eliason, William K.
AU - Steitz, Thomas A.
PY - 2007/10/19
Y1 - 2007/10/19
N2 - The complex between the DnaB helicase and the DnaG primase unwinds duplex DNA at the eubacterial replication fork and synthesizes the Okazaki RNA primers. The crystal structures of hexameric DnaB and its complex with the helicase binding domain (HBD) of DnaG reveal that within the hexamer the two domains of DnaB pack with strikingly different symmetries to form a distinct two-layered ring structure. Each of three bound HBDs stabilizes the DnaB hexamer in a conformation that may increase its processivity. Three positive, conserved electrostatic patches on the N-terminal domain of DnaB may also serve as a binding site for DNA and thereby guide the DNA to a DnaG active site.
AB - The complex between the DnaB helicase and the DnaG primase unwinds duplex DNA at the eubacterial replication fork and synthesizes the Okazaki RNA primers. The crystal structures of hexameric DnaB and its complex with the helicase binding domain (HBD) of DnaG reveal that within the hexamer the two domains of DnaB pack with strikingly different symmetries to form a distinct two-layered ring structure. Each of three bound HBDs stabilizes the DnaB hexamer in a conformation that may increase its processivity. Three positive, conserved electrostatic patches on the N-terminal domain of DnaB may also serve as a binding site for DNA and thereby guide the DNA to a DnaG active site.
UR - http://www.scopus.com/inward/record.url?scp=35348979683&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=35348979683&partnerID=8YFLogxK
U2 - 10.1126/science.1147353
DO - 10.1126/science.1147353
M3 - Article
C2 - 17947583
AN - SCOPUS:35348979683
VL - 318
SP - 459
EP - 463
JO - Science
JF - Science
SN - 0036-8075
IS - 5849
ER -